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- PDB-1bh7: A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, ... -

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Basic information

Entry
Database: PDB / ID: 1bh7
TitleA LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsBAND 3Band 3 anion transport protein
KeywordsMEMBRANE PROTEIN / CYTOPLASMIC LOOP / ANION EXCHANGE PROTEIN
Function / homology
Function and homology information


pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / negative regulation of urine volume / Bicarbonate transporters / intracellular monoatomic ion homeostasis / ankyrin-1 complex / plasma membrane phospholipid scrambling / monoatomic anion transmembrane transporter activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity ...pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / negative regulation of urine volume / Bicarbonate transporters / intracellular monoatomic ion homeostasis / ankyrin-1 complex / plasma membrane phospholipid scrambling / monoatomic anion transmembrane transporter activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / bicarbonate transmembrane transporter activity / bicarbonate transport / monoatomic anion transport / chloride transport / chloride transmembrane transporter activity / erythrocyte development / negative regulation of glycolytic process through fructose-6-phosphate / ankyrin binding / hemoglobin binding / cortical cytoskeleton / protein-membrane adaptor activity / chloride transmembrane transport / protein localization to plasma membrane / regulation of intracellular pH / transmembrane transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / cytoplasmic side of plasma membrane / Z disc / blood coagulation / basolateral plasma membrane / blood microparticle / protein homodimerization activity / extracellular exosome / membrane / plasma membrane
Similarity search - Function
Anion exchange protein 1 / Anion exchange protein / Anion exchange, conserved site / Anion exchangers family signature 1. / Anion exchangers family signature 2. / Band 3 cytoplasmic domain / Band 3 cytoplasmic domain / Bicarbonate transporter, eukaryotic / Bicarbonate transporter-like, transmembrane domain / HCO3- transporter family / Phosphotransferase/anion transporter
Similarity search - Domain/homology
Band 3 anion transport protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsAskin, D. / Bloomberg, G.B. / Chambers, E.J. / Tanner, M.J.A.
CitationJournal: Biochemistry / Year: 1998
Title: NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Authors: Askin, D. / Bloomberg, G.B. / Chambers, E.J. / Tanner, M.J.
History
DepositionJun 16, 1998Processing site: BNL
Revision 1.0Nov 4, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BAND 3


Theoretical massNumber of molelcules
Total (without water)4,1581
Polymers4,1581
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 15AVERAGE STRUCTURE- ONLY THE THREE STRUCTURED REGIONS WITHIN THE PEPTIDE ARE GIVEN
Representative

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Components

#1: Protein/peptide BAND 3 / Band 3 anion transport protein


Mass: 4158.074 Da / Num. of mol.: 1 / Fragment: FINAL CYTOPLASMIC LOOP
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P02730

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121COSY
131HOHAHA
NMR detailsText: THE STRUCTURE WAS DETERMINED USING 2D SOLUTION-STATE NMR

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Sample preparation

DetailsContents: 30% TFE-D3/H2O
Sample conditionsIonic strength: 12mM / pH: 3.5 / Pressure: ATMOSPHERIC atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: JEOL ALPHA 500MHZ / Manufacturer: JEOL / Model: ALPHA 500MHZ / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
Details: 480 DISTANCE RESTRAINTS 10 DIHEDRAL ANGLE RESTRAINTS 4 H-BONDING DISTANCE RESTRAINTS NO NOE VIOLATIONS > 0.05NM NO TORSION ANGLE VIOLATIONS > 5 DEGREES
NMR ensembleConformer selection criteria: AVERAGE STRUCTURE- ONLY THE THREE STRUCTURED REGIONS WITHIN THE PEPTIDE ARE GIVEN
Conformers calculated total number: 15 / Conformers submitted total number: 1

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